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Gerner"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Acute Leukemia"],"software":[""],"submitter_keywords":["protac","metallo-protac","targeted protein degradation","degradome","protein half-life","Cancer","Cancer; degradome; metallo-protac; protac; protein half-life; targeted protein degradation"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067054"],"tissue":["Hl-60 Cell","Blood"],"sample_protocol":["Differentiation of HL-60 cells (500’000 cells) was performed in 6-well plates and induced by PMA (100 ng∙mL-1) over 72 h. Cells were then treated with complete culture medium (200 µL) containing either solvent vehicle control (DMSO or EtOH), CHX (10 µM), ACBI2 (1 nM + 10 µM CHX) or AuPROTAC (60 µM + 10 µM CHX) in triplicates. Whole cell lysates were obtained after 0.5, 1, 2, 4 and 8 h incubation. Control cells were additionally harvested directly at the beginning of the experiment (t = 0). Additionally, PMA-differentiated HL-60 cells were treated with bortezomib (4h, 25 nM) after which ACBI2 (1 nM) or AuPROTAC (60 µM) was added for another 4 h. Whole cell lysates were generated by removing medium and washing the wells twice with cold PBS (2 mL). Cells were scraped, lysed in SDC buffer and heated to 95 °C for 5 mins at 1400 rpm. Protein quantification in sample lysates was performed by means of the Bicinchoninic acid (BCA) colorimetric assay and samples were adjusted to 20 µg protein. Whole cell lysates were proteolytically digested according to an in-solution digestion protocol, followed by StageTip desalting. In brief, reduction/alkylation buffer contained TCEP (200 mM stock) and 2-chlroacetamide (800 µM stock) was added. After reaching RT, trypsin/Lys-C (1 µL, 0.2 µg∙µL-1, enzyme-to-substrate ratio of 1 : 100) was added to each sample and incubated for 17 h on a thermoshaker (1400 rpm, 30 °C). Then, the samples were nearly dried in a vacuum concentrator (40 min, 40 °C). The StageTips were prepared by stacking two disks of a polystyrenedivinylbenzene-reversed phase sulfonate material (Empore 2241 SDB-RPS, 12 µm particle size, 47mm; CDS Analytical LLC) into a pipet tip. After washing, the samples were transferred onto the tips and centrifuged. After loading buffer/wash buffer 1 and SDB-RPS wash buffer 2, the peptides were eluted into a glass inlet. The samples were finally dried in the vacuum concentrator (40 °C). Dried peptide samples were reconstituted in loading solvent (40 µL, 97.95% water, 2% acetonitrile, 0.05% TFA) and synthetic peptide standards (5 µL, 10 fmol∙µL-1, in 30% FA) were added. Chromatography was performed on a Dionex UltiMate 3000 RSLCnano system (Thermo Fisher Scientific). The injection volume was 5 µL and the pre-column was Acclaim PepMap C18 100 (Thermo Fisher Scientific). Solvent A was 99.9% water, 0.1% formic acid. Peptides were separated on an Aurora emitter column (1.6 µm C18, 25 cm × 75 µm, IonOpticks) by applying a gradient ranging from 12% to 42% solvent B (79.9% acetonitrile, 20% water, 0.1% FA) over the course of 90 min at a flow rate of 300 nL∙min-1. Mass spectrometric analysis was performed on a timsTOF Pro (Bruker Daltonics) mass spectrometer running in parallel accumulation-serial fragmentation (PASEF) mode and data dependent acquisition (DDA). An m/z scan range of 100–1700 was set to acquire MS1 and MS2 spectra. An inverse reduced ion mobility (1/k0) scan ranging from 0.6–1.6 V∙s∙cm2 contributed to a total ramp time of 100 ms to achieve trapped ion mobility separation. The total cycle time was 1.16 s, including 10 PASEF MS/MS scans per cycle."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The acquired data was processed using MaxQuant (version 1.6.17.0) with the Andromeda search engine to enable identification and label-free quantification (LFQ) of proteins and searched against the SwissProt homo sapiens database (14.12.2019 with 20380 canonical entries). False discovery rates for peptide-spectrum match (PSM) and protein were set to 0.01, the \"match between runs\" setting was enabled with a matching time window of 0.7 min and an alignment time window of 20 min. Further criteria included a MS/MS mass tolerance of 40 ppm and a maximum of two missed cleavages. A minimal requirement for protein identification was set to one unique peptide. Carbamidomethylation of cysteine was set as fixed modification while methionine oxidation and the acetylation of the protein N-terminus were included in the search as variable modifications. Perseus (version 1.6.14.0) was used for filtering and imputation. First, proteins only identified by site, common contaminants as well as proteins matching reversed sequences were filtered out. LFQ-values of remaining entries were log2-transformed.  Entries with missing values were then imputed with values from a normal distribution (downshift: 1.8, width: 0.3). Volcano plots were generated using a two-sided t-tests with a s0 = 0.1, FDR = 0.05 and 250 permutations. Data matrices prior and after replacement of missing values were exported from Perseus and imported to Python (version 3.11.5) for further filtering steps, analysis and plotting. The Pandas package was used for the bulk of data processing, while the Matplotlib and Seaborn packages were employed for data plotting."],"omics_type":["Proteomics"],"labhead":["Christopher Gerner"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["University of Vienna, Faculty of Chemistry, Department of Analytical Chemistry"],"species":["Homo Sapiens (human)"],"publication":["10.1021/ACSCHEMBIO.5C00860"],"submitter_mail":["christopher.gerner@univie.ac.at"],"submitter_affiliation":["University of Vienna"],"submitter_country":["Austria"],"additional_accession":[]},"is_claimable":false,"name":"A Gold-PROTAC degrades the oncogenic tyrosine kinase MERKT: Insights into the degradome from a steady-state system","description":"Targeted protein degradation is a valuable strategy to eliminate disease-relevant proteins. Among other classes, proteolysis targeting chimeras (PROTACs) are bifunctional molecules that induce the proximity of a recruiter E3 ligase and the target protein of interest for ubiquitination and subsequent degradation by the proteasome. While most PROTACs are non-covalent interactors, covalent PROTACs may benefit from increased selectivity and altered pharmacodynamics, yet remain largely understudied. In this context, a gold-based metallo-PROTAC (AuPROTAC) was synthesized, consisting of a cyclometalated Au(III) complex based on a bidentate C^N-ligand, which induces covalent cysteine/selenocysteine-arylation in a gold-templated two-step mechanism. This was then linked to a cereblon binding moiety. The degradome of the covalent AuPROTAC was characterized by establishing a cycloheximide chase assay, which was performed in a non-proliferative steady-state cell culture system that maintained a static protein turnover and efficiently decouples protein degradation from down-regulation. The method was verified with the known SMARCA2 and PBRM1-degrader ACBI2. The AuPROTAC was found to degrade MERTK and TXNL1, while their degradation was successfully rescued by proteasome inhibition. Since MERTK does not contain a cysteine in the active binding pocket, AuPROTAC is believed to covalently modify this protein at an allosteric site, leading to its degradation by the proteasome. The PROTACs were found to affect protein half-lives in this cycloheximide chase assay. Therefore, proteome-wide degradation selectivity was further characterized by ranking degraded targets based on the acceleration of protein half-lives. Overall, the established approach can be used to efficiently explore degradomes of CRBN and VHL recruiter-based PROTACs.","dates":{"publication":"2026-07-27","submission":"2025-08-07"},"accession":"PXD067054","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:22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